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Q2UFP8 (BGLC_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable beta-glucosidase C

EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase C
Cellobiase C
Gentiobiase C
Gene names
Name:bglC
ORF Names:AO090026000123
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length638 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose By similarity.

Catalytic activity

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

Pathway

Glycan metabolism; cellulose degradation.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 3 family.

Sequence caution

The sequence BAE59617.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 638620Probable beta-glucosidase C
PRO_0000394104

Sites

Active site3411 By similarity

Amino acid modifications

Glycosylation401N-linked (GlcNAc...) Potential
Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation2231N-linked (GlcNAc...) Potential
Glycosylation2741N-linked (GlcNAc...) Potential
Glycosylation3641N-linked (GlcNAc...) Potential
Glycosylation4801N-linked (GlcNAc...) Potential
Glycosylation4881N-linked (GlcNAc...) Potential
Glycosylation5281N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q2UFP8 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: F070472F086BA6F1

FASTA63870,451
        10         20         30         40         50         60 
MKVLAPGYLA EASLTALASG CQALSTRPYV PRGYSLSRRN DSTPIYKDAS YCIDERVDDL 

        70         80         90        100        110        120 
LARMTIEEKA GQLFHTRLMD GPLDDEGSGN NAHNSTSNMI GEKHMTHFNL ASDITNATET 

       130        140        150        160        170        180 
AEFINRIQEL ALQTRLGIPV TVSTDPRHSF TENVGTGFKA GVFSQWPESI GLAALRDPYV 

       190        200        210        220        230        240 
VRKFAEVAKE EYIAVGIRAA LHPQVDLSTE PRWARISNTW GENSTLTSEL LVEYIKGFQG 

       250        260        270        280        290        300 
DKLGPQSVKT VTKHFPGGGP VENGEDSHFA YGKNQTYPGN NLEEHLKPFK AAIAAGATEI 

       310        320        330        340        350        360 
MPYYSRPIGT EYEPVAFSFN KRIVTELLRN ELGFDGIVLT DWGLITDGYI AGQYMPARAW 

       370        380        390        400        410        420 
GVENLTELQR AARILDAGCD QFGGEERPEL IVQLVQEGII SEDRIDVSVR RLLKEKFVLG 

       430        440        450        460        470        480 
LFDNPFVDAE AAGRVVGNDY FVRLGREAQR RSYTLLSNNE DIVPLKKIEK STKFYIEGFN 

       490        500        510        520        530        540 
ASFIESWNYT VVDSPEEAEY ALLRYNAPYE PRPGGFEANM HAGSLAFNDT EKARQAKIYS 

       550        560        570        580        590        600 
AVPTIVDIVM DRPAVIPEII EQAKAVFASY GSDSNAFLDV VFGVSAPEGK LPFDLPSSME 

       610        620        630 
AVEAQMEDVP FDTRNPVFKF GHGLSYANPC ASSSSKCS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007159 Genomic DNA. Translation: BAE59617.1. Different initiation.

3D structure databases

ProteinModelPortalQ2UFP8.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000285275.
OrthoDBEOG7R8394.

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

Gene3D3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProIPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR30620. PTHR30620. 1 hit.
PfamPF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSPR00133. GLHYDRLASE3.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBGLC_ASPOR
AccessionPrimary (citable) accession number: Q2UFP8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: May 18, 2010
Last modified: February 19, 2014
This is version 42 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries